y
Basic Information | |
---|---|
Species | Cucumis sativus |
Cazyme ID | Cucsa.378410.2 |
Family | GH13 |
Protein Properties | Length: 849 Molecular Weight: 95989 Isoelectric Point: 4.6172 |
Chromosome | Chromosome/Scaffold: 03810 Start: 26811 End: 42474 |
Description | starch branching enzyme 2.1 |
View CDS |
External Links |
---|
NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
GH13 | 328 | 648 | 1.6e-28 |
LPRIKKLGYNAVQIMAIQEHSYYASFGYHVTNFFAPSSRCGTPEELKSLIDRAHELGLLVLMDIVHSHASKNVLDGLNMFDGTDGHYFHSGSRGYHWMWD SRLFNYGSWEVLRYLLSNARWWLEEYKFDGFRFDGVTSMMYTHHGLEVGFTGNYSEYFGFATDVDAVVYLMLVNDMIHGLYPEAVTIGEDVSGMPTFCIP VQDGGIGFDYRLHMAIADKWIELLKKSDEDWEMGEIVHTLVNRRWLENCVAYAESHDQALVGDKTVAFWLMDKDMYDSMALDRPSTPAIDRGIALHKMIR LITMGLGGEGYLNFMGNEFGH |
Full Sequence |
---|
Protein Sequence Length: 849 Download |
MVYTISGIRF PAVPPLCKRS DSTFNGDRRM PLSLFMKKDS SPRRIFVTKS TYDSDSVSST 60 ATAASDKVLV PGSGSDGSST LAGQSENYGA VSEDPQVLPD IDSQIIEAHE KTKEETDQDP 120 ESLPVDNIDG DQAPLEEISI PSKNKKAETT VRSIPPPGSG QRIYDIDPYL LSHRGHLDYR 180 YGQYIRMREA IDQNEGGLEA FSRGYEKFGF TRSATGITYR EWAPGAKSAA LIGDFNNWNP 240 NADIMSRNEF GVWEIFLPNN ADGSPAIPHG SRVKIRMDTP SGIKDSIPAW IKFSVQAPGE 300 IPYNGIYYDP PEEEPIINSY ANFRDDVLPR IKKLGYNAVQ IMAIQEHSYY ASFGYHVTNF 360 FAPSSRCGTP EELKSLIDRA HELGLLVLMD IVHSHASKNV LDGLNMFDGT DGHYFHSGSR 420 GYHWMWDSRL FNYGSWEVLR YLLSNARWWL EEYKFDGFRF DGVTSMMYTH HGLEVGFTGN 480 YSEYFGFATD VDAVVYLMLV NDMIHGLYPE AVTIGEDVSG MPTFCIPVQD GGIGFDYRLH 540 MAIADKWIEL LKKSDEDWEM GEIVHTLVNR RWLENCVAYA ESHDQALVGD KTVAFWLMDK 600 DMYDSMALDR PSTPAIDRGI ALHKMIRLIT MGLGGEGYLN FMGNEFGHPE WIDFPRGDQH 660 LPGGAVIPGN NFSYDKCRRR FDLGDADYLR YHGMQEFDRA MQHLEESFGF MTAGHQYVSR 720 KDDRDKIIVF ERGDLVFVFN FHWSNSYYDY RVGCLKPGKY KIVLDSDDPL FGGYNRLDHS 780 AEYFTFEGNY DNRPRSFLIY APSRTAVVYA LAPDDSELAN GETEAITETE TESETETETE 840 TETETSLE* 900 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 6.0e-8 | 141 | 257 | 132 | + alpha-amylase | ||
PLN03244 | PLN03244 | 6.0e-127 | 265 | 812 | 554 | + alpha-amylase; Provisional | ||
PLN02960 | PLN02960 | 1.0e-169 | 265 | 812 | 581 | + alpha-amylase | ||
PLN02447 | PLN02447 | 0 | 95 | 820 | 758 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 313 | 699 | 388 | + Alpha amylase catalytic domain found in bacterial and eukaryotic branching enzymes. Branching enzymes (BEs) catalyze the formation of alpha-1,6 branch points in either glycogen or starch by cleavage of the alpha-1,4 glucosidic linkage yielding a non-reducing end oligosaccharide chain, and subsequent attachment to the alpha-1,6 position. By increasing the number of non-reducing ends, glycogen is more reactive to synthesis and digestion as well as being more soluble. This group includes bacterial and eukaryotic proteins. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase. |
Gene Ontology | |
---|---|
GO Term | Description |
GO:0003824 | catalytic activity |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005975 | carbohydrate metabolic process |
GO:0043169 | cation binding |
Annotations - NR Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | ABO31358.1 | 0 | 1 | 812 | 1 | 839 | starch branching enzyme II-1 [Malus x domestica] |
GenBank | ABO31359.1 | 0 | 1 | 811 | 1 | 838 | starch branching enzyme II-2 [Malus x domestica] |
GenBank | ACA35282.1 | 0 | 1 | 712 | 1 | 769 | starch branching enzyme I [Cucumis sativus] |
GenBank | ACA35286.1 | 0 | 1 | 826 | 1 | 883 | starch branching enzyme I [Cucumis sativus] |
EMBL | CAA56319.1 | 0 | 1 | 842 | 1 | 885 | starch branching enzyme I [Pisum sativum] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3aml_A | 0 | 163 | 843 | 13 | 725 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3amk_A | 0 | 163 | 817 | 13 | 698 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 163 | 817 | 13 | 698 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 163 | 817 | 13 | 698 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 1m7x_D | 7.00649e-43 | 214 | 775 | 24 | 579 | A Chain A, The X-Ray Crystallographic Structure Of Branching Enzyme |
EST Download unfiltered results here | ||||
---|---|---|---|---|
Hit | Length | Start | End | EValue |
HO794536 | 686 | 157 | 814 | 0 |
HO777638 | 630 | 213 | 814 | 0 |
HO458123 | 393 | 418 | 810 | 0 |
HO458123 | 296 | 157 | 417 | 0 |
HO777638 | 47 | 166 | 212 | 0.0000000007 |
Sequence Alignments (This image is cropped. Click for full image.) |
---|
![]() |